6OI4: RPN13 (19-132)-RPN2 (940-952) pY950-Ub complex

RPN13 (19-132)-RPN2 (940-952) pY950-Ub complex. Determined by X-ray diffraction at 1.76 Å resolution. Released 15 May 2019.

Method: X-ray diffraction
Resolution: 1.76 Å
Organism: Homo sapiens
Chains: 6
Atoms: 3,593
Mol. weight: 47.84 kDa
Released: 15 May 2019

Explore 6OI4 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6OI4 contains 14 α-helices and 34 β-strands across 6 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain A: 2 helices, 9 β-strands

Element	Residues	Length	Sheet
β-strand	24-27	4	1
β-strand	28-34	7	2
β-strand	37-40	4	2
β-strand	45-51	7	1
β-strand	57-63	7	1
β-strand	69-75	7	1
β-strand	80-84	5	2
β-strand	93-98	6	2
α-helix	99-101	3
β-strand	104-109	6	2
α-helix	117-129	13

Chain B: 1 helix, 9 β-strands

Element	Residues	Length	Sheet
β-strand	24-27	4	5
β-strand	28-34	7	6
β-strand	37-40	4	6
β-strand	45-51	7	5
β-strand	57-63	7	5
β-strand	69-74	6	5
β-strand	80-84	5	6
β-strand	93-98	6	6
β-strand	104-109	6	6
α-helix	117-129	13

Chain C: 4 helices, 7 β-strands

Element	Residues	Length	Sheet
β-strand	2-7	6	3
β-strand	12-16	5	3
β-strand	22	1	4
α-helix	23-34	12
α-helix	38-40	3
β-strand	41-45	5	3
β-strand	48-49	2	3
α-helix	50-51	2
β-strand	55	1	4
α-helix	57-59	3
β-strand	66-71	6	3

Chain D: 5 helices, 7 β-strands

Element	Residues	Length	Sheet
β-strand	2-7	6	7
β-strand	12-16	5	7
β-strand	22	1	8
α-helix	23-34	12
α-helix	38-40	3
β-strand	41-45	5	7
β-strand	48-49	2	7
α-helix	50-51	2
β-strand	55	1	8
α-helix	57-59	3
α-helix	61-62	2
β-strand	66-71	6	7

Chains E and F: 1 helix, 1 β-strand

Element	Residues	Length	Sheet
α-helix	941-947	7
β-strand	948-949	2	2

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Proteasomal ubiquitin receptor ADRM1	A, B	protein	113	Homo sapiens	Q16186 (AlphaFold model)
ubiquitin	C, D	protein	76	Homo sapiens	P0CG48 (AlphaFold model)
26S proteasome non-ATPase regulatory subunit 1	E, F	protein	14	Homo sapiens	Q99460 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>6OI4_1 Proteasomal ubiquitin receptor ADRM1 (chains A, B)
NKYLVEFRAGKMSLKGTTVTPDKRKGLVYIQQTDDSLIHFCWKDRTSGNVEDDLIIFPDD
CEFKRVPQCPSGRVYVLKFKAGSKRLFFWMQEPKTDQDEEHCRKVNEYLNNPP

Sequence of entity 2 (C, D), FASTA

>6OI4_2 ubiquitin (chains C, D)
MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYN
IQKESTLHLVLRLRGG

Sequence of entity 3 (E, F), FASTA

>6OI4_3 26S proteasome non-ATPase regulatory subunit 1 (chains E, F)
PQEPEPPEPFEYID

Primary citation

Phosphorylation of Tyr-950 in the proteasome scaffolding protein RPN2 modulates its interaction with the ubiquitin receptor RPN13. Hemmis, C.W., Heard, S.C., Hill, C.P. J Biol Chem (2019) 294:9659-9665. DOI 10.1074/jbc.AC119.008881 · PubMed

Other PDB entries of the same protein (UniProt Q16186 (AlphaFold model), which also has an AlphaFold model), best resolution first:

5V1Y 1.42 Å, Crystal structure of the ternary RPN13 PRU-RPN2 (940-953)-ubiquitin complex
5IRS 1.8 Å, crystal structure of the proteasomal Rpn13 PRU-domain
8VWO 1.85 Å, Crystal structure of hRpn13 Pru bound with U-shaped peptide
4WLR 2.0 Å, Crystal Structure of mUCH37-hRPN13 CTD-hUb complex
5V1Z 2.0 Å, Crystal structure of the RPN13 PRU-RPN2 (932-953)-ubiquitin complex
8FTQ 2.1 Å, Crystal structure of hRpn13 Pru domain in complex with Ubiquitin and XL44
4UEL 2.3 Å, UCH-L5 in complex with ubiquitin-propargyl bound to the RPN13 DEUBAD domain
9E7K 2.41 Å, Crystal structure of the UCH37 RPN13 DEUBAD complex bound to an inhibitory nanobody in…
4UEM 2.82 Å, UCH-L5 in complex with the RPN13 DEUBAD domain
4WLQ 2.85 Å, Crystal structure of mUCH37-hRPN13 CTD complex
2KQZ Solution structure of the Rpn13 DEUBAD domain
2KR0 Solution structure of the proteasome ubiquitin receptor Rpn13

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